CADH2_ORYSJ
ID CADH2_ORYSJ Reviewed; 363 AA.
AC Q6ZHS4; A0A0N7KEU2; Q75W59;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Cinnamyl alcohol dehydrogenase 2 {ECO:0000305};
DE Short=OsCAD2 {ECO:0000303|PubMed:15452707};
DE EC=1.1.1.195 {ECO:0000269|PubMed:16443696};
DE AltName: Full=Protein GOLD HULL AND INTERNODE 2 {ECO:0000303|PubMed:16443696};
GN Name=CAD2 {ECO:0000303|PubMed:15452707};
GN Synonyms=CAD, GH2 {ECO:0000303|PubMed:16443696};
GN OrderedLocusNames=Os02g0187800, LOC_Os02g09490;
GN ORFNames=OJ1073_F05.31, OJ1145_F01.6;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 206-363.
RC STRAIN=cv. Fujiminori;
RA Mase K., Nishikubo N., Satou K., Nakano Y., Kajita S., Katayama Y.;
RT "The cDNA encoding cinnamyl alcohol dehydrogenase in rice stem.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION, TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15452707; DOI=10.1007/s00425-004-1385-4;
RA Tobias C.M., Chow E.K.;
RT "Structure of the cinnamyl-alcohol dehydrogenase gene family in rice and
RT promoter activity of a member associated with lignification.";
RL Planta 220:678-688(2005).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-185.
RX PubMed=16443696; DOI=10.1104/pp.105.073007;
RA Zhang K., Qian Q., Huang Z., Wang Y., Li M., Hong L., Zeng D., Gu M.,
RA Chu C., Cheng Z.;
RT "GOLD HULL AND INTERNODE2 encodes a primarily multifunctional cinnamyl-
RT alcohol dehydrogenase in rice.";
RL Plant Physiol. 140:972-983(2006).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=21912859; DOI=10.1007/s00299-011-1142-7;
RA Hirano K., Aya K., Kondo M., Okuno A., Morinaka Y., Matsuoka M.;
RT "OsCAD2 is the major CAD gene responsible for monolignol biosynthesis in
RT rice culm.";
RL Plant Cell Rep. 31:91-101(2012).
CC -!- FUNCTION: Involved in lignin biosynthesis (PubMed:16443696,
CC PubMed:21912859). Catalyzes the final step specific for the production
CC of lignin monomers. Catalyzes the NADPH-dependent reduction of
CC coniferaldehyde and sinapaldehyde to their respective alcohols
CC (PubMed:16443696). Plays the major role in monolignol biosynthesis.
CC Functions cooperatively with COMT in the culm internodes for the
CC biosynthesis of monolignols, the lignin precursors. May be involved in
CC lignin biosynthesis in leaves and roots (PubMed:21912859).
CC {ECO:0000269|PubMed:16443696, ECO:0000269|PubMed:21912859}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-cinnamyl alcohol + NADP(+) = (E)-cinnamaldehyde + H(+) +
CC NADPH; Xref=Rhea:RHEA:10392, ChEBI:CHEBI:15378, ChEBI:CHEBI:16731,
CC ChEBI:CHEBI:33227, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.195; Evidence={ECO:0000269|PubMed:16443696};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:O49482};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:O49482};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.4 uM for coniferaldehyde {ECO:0000269|PubMed:16443696};
CC KM=20.8 uM for sinapaldehyde {ECO:0000269|PubMed:16443696};
CC Vmax=32.9 pmol/sec/ug enzyme with coniferaldehyde as substrate
CC {ECO:0000269|PubMed:16443696};
CC Vmax=87.0 pmol/sec/ug enzyme with sinapaldehyde as substrate
CC {ECO:0000269|PubMed:16443696};
CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O49482}.
CC -!- TISSUE SPECIFICITY: Expressed in roots behind the root tips in the
CC pericycle region and layer of cortical cells adjacent to the exodermis.
CC Expressed in vascular bundles and lateral veins of leaf sheaths and
CC blades. Expressed in the vicinity of vascular bundles in the first
CC internode below the inflorescence (PubMed:15452707, PubMed:16443696).
CC Highly expressed in the culm (PubMed:21912859).
CC {ECO:0000269|PubMed:15452707, ECO:0000269|PubMed:16443696,
CC ECO:0000269|PubMed:21912859}.
CC -!- DISRUPTION PHENOTYPE: Reduced lignin content, reddish-brown coloration
CC of panicles and internodes, and golden yellow seeds.
CC {ECO:0000269|PubMed:16443696}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AP003990; BAD15428.1; -; Genomic_DNA.
DR EMBL; AP004046; BAD15519.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF08046.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS77369.1; -; Genomic_DNA.
DR EMBL; AK105011; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AB122054; BAD14921.1; -; mRNA.
DR EMBL; BK003969; DAA02237.1; -; Genomic_DNA.
DR RefSeq; XP_015626408.1; XM_015770922.1.
DR AlphaFoldDB; Q6ZHS4; -.
DR SMR; Q6ZHS4; -.
DR STRING; 4530.OS02T0187800-01; -.
DR PaxDb; Q6ZHS4; -.
DR PRIDE; Q6ZHS4; -.
DR EnsemblPlants; Os02t0187800-01; Os02t0187800-01; Os02g0187800.
DR GeneID; 4328552; -.
DR Gramene; Os02t0187800-01; Os02t0187800-01; Os02g0187800.
DR KEGG; osa:4328552; -.
DR eggNOG; KOG0023; Eukaryota.
DR InParanoid; Q6ZHS4; -.
DR OMA; LPWIQKR; -.
DR OrthoDB; 625659at2759; -.
DR BRENDA; 1.1.1.195; 8948.
DR PlantReactome; R-OSA-1119316; Phenylpropanoid biosynthesis.
DR SABIO-RK; Q6ZHS4; -.
DR UniPathway; UPA00711; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR ExpressionAtlas; Q6ZHS4; baseline and differential.
DR Genevisible; Q6ZHS4; OS.
DR GO; GO:0045551; F:cinnamyl-alcohol dehydrogenase activity; IDA:Gramene.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0052747; F:sinapyl alcohol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009809; P:lignin biosynthetic process; IDA:Gramene.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW Lignin biosynthesis; Metal-binding; NADP; Oxidoreductase;
KW Reference proteome; Zinc.
FT CHAIN 1..363
FT /note="Cinnamyl alcohol dehydrogenase 2"
FT /id="PRO_0000382641"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 49
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 167
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 188..193
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 211..216
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 251
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 275
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 298..300
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT MUTAGEN 185
FT /note="G->D: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16443696"
FT CONFLICT 293
FT /note="K -> E (in Ref. 4; AK105011)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 363 AA; 38644 MW; EFD21231AFB35B4B CRC64;
MGSLAAEKTV TGWAARDASG HLTPYNYTLR KTGPEDVVVK VLYCGICHTD IHQAKNHLGA
SKYPMVPGHE VVGEVVEVGP EVTKYSAGDV VGVGVIVGCC RECHPCKANV EQYCNKRIWS
YNDVYTDGRP TQGGFASAMV VDQKFVVKIP AGLAPEQAAP LLCAGLTVYS PLKHFGLMSP
GLRGGVLGLG GVGHMGVKVA KSMGHHVTVI SSSARKRGEA MDDLGADAYL VSSDAAAMAA
AGDSLDYIID TVPVHHPLEP YLALLKLDGK LILMGVINQP LSFISPMVML GRKAITGSFI
GSMAETEEVL NFCVDKGLTS QIEVVKMDYV NQALERLERN DVRYRFVVDV AGSNIDDADA
PPA
